CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001601
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Activator of 90 kDa heat shock protein ATPase homolog 1 
Protein Synonyms/Alias
 AHA1; p38 
Gene Name
 AHSA1 
Gene Synonyms/Alias
 C14orf3; HSPC322 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MAKWGEGDPRacetylation[1]
3*****MAKWGEGDPRubiquitination[2]
94LNWTGTSKSGVQYKGubiquitination[3, 4, 5]
203QARPVGVKIPTCKITubiquitination[2]
208GVKIPTCKITLKETFubiquitination[2, 4]
212PTCKITLKETFLTSPacetylation[1]
212PTCKITLKETFLTSPubiquitination[2, 3, 5]
249LEADRGGKFHMVDGNubiquitination[3, 5]
328RYYFEGIKQTFGYGAubiquitination[2, 3, 4, 5, 6]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 3 3 N6-acetyllysine.
 MOD_RES 193 193 Phosphoserine.
 MOD_RES 212 212 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm; Endoplasmic reticulum; Phosphoprotein; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 338 AA 
Protein Sequence
MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ NEEGKCEVTE 60
VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK GHVEIPNLSD ENSVDEVEIS 120
VSLAKDEPDT NLVALMKEEG VKLLREAMGI YISTLKTEFT QGMILPTMNG ESVDPVGQPA 180
LKTEERKAKP APSKTQARPV GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA 240
TLEADRGGKF HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL 300
CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF 338 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
 GO:0051087; F:chaperone binding; IDA:MGI.
 GO:0006457; P:protein folding; ISS:UniProtKB.
 GO:0006950; P:response to stress; ISS:UniProtKB. 
Interpro
 IPR013538; Activator_of_Hsp90_ATPase.
 IPR015310; AHSA1_N.
 IPR023393; START-like_dom. 
Pfam
 PF09229; Aha1_N
 PF08327; AHSA1 
SMART
 SM01000; Aha1_N 
PROSITE
  
PRINTS